tepsin Inhibitors

Tepsin inhibitors like compounds like Brefeldin A, Monensin, and Golgicide A disrupt the structure and function of the Golgi apparatus and endosomes, which are critical for the endosome-to-Golgi retrieval pathway that tepsin is known to participate in. The integrity and function of these organelles are essential for tepsin to mediate its role in cargo selection and sorting.

Additionally, inhibitors that perturb the cytoskeleton, such as Nocodazole, Cytochalasin D, Latrunculin A, and ML141, alter the transport and organization of vesicles, which is a key aspect of tepsin's involvement in cellular trafficking. Nocodazole and Paclitaxel have opposing effects on microtubules, yet both result in altered vesicle transport dynamics that are necessary for tepsin's function. Cytochalasin D and Latrunculin A target actin filaments, which are also implicated in maintaining the vesicular trafficking pathways where tepsin operates. Other inhibitors, such as Dynasore, Chlorpromazine, and Pitstop 2, specifically target the endocytic machinery. By inhibiting dynamin or blocking clathrin-mediated endocytosis, these compounds can disrupt the endosomal sorting processes that tepsin is a part of. Lastly, Genistein broadly targets signaling pathways by inhibiting tyrosine kinases, leading to alterations in the signaling that may govern tepsin's activity in protein sorting.